| + |
ATM | up-regulates activity 
phosphorylation
|
DCK |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275798 |
Ser74 |
EFEELTMsQKNGGNV |
|
|
| pmid |
sentence |
| 27879648 |
Deoxycytidine kinase (dCK) is a key enzyme in deoxyribonucleoside salvage and the anti-tumor activity for many nucleoside analogs. dCK is activated in response to ionizing radiation (IR)-induced DNA damage and it is phosphorylated on Serine 74 by the Ataxia-Telangiectasia Mutated (ATM) kinase in order to activate the cell cycle G2/M checkpoint. |
|
| Publications: |
1 |
| + |
PP2CA_R1A_R2A | down-regulates activity 
dephosphorylation
|
DCK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275804 |
Ser74 |
EFEELTMsQKNGGNV |
|
|
| pmid |
sentence |
| 24462681 |
Protein phosphatase 2A regulates deoxycytidine kinase activity via Ser-74 dephosphorylation|Deoxycytidine kinase (dCK) is a critical enzyme for activation of anticancer nucleoside analogs. Its activity is controlled via Ser-74 phosphorylation. Here, we investigated which Ser/Thr phosphatase dephosphorylates Ser-74. In cells, the PP1/PP2A inhibitor okadaic acid increased both dCK activity and Ser-74 phosphorylation |
|
| Publications: |
1 |
| + |
DCK | up-regulates 
phosphorylation
|
G2/M_transition-checkpoint |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275806 |
Ser74 |
|
|
|
| pmid |
sentence |
| 27879648 |
Deoxycytidine kinase (dCK) is a key enzyme in deoxyribonucleoside salvage and the anti-tumor activity for many nucleoside analogs. dCK is activated in response to ionizing radiation (IR)-induced DNA damage and it is phosphorylated on Serine 74 by the Ataxia-Telangiectasia Mutated (ATM) kinase in order to activate the cell cycle G2/M checkpoint. |
|
| Publications: |
1 |
| + |
CSNK1D | up-regulates activity
phosphorylation
|
DCK |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275799 |
Ser74 |
EFEELTMsQKNGGNV |
|
|
| pmid |
sentence |
| 20637175 |
We showed that recombinant CKI delta phosphorylated several residues of bacterially overexpressed dCK: Ser-74, but also Ser-11, Ser-15, and Thr-72. Phosphorylation of dCK by CKI delta correlated with increased activity reaching at least 4-fold. Site-directed mutagenesis demonstrated that only Ser-74 phosphorylation was involved in dCK activation by CKI delta, |
|
| Publications: |
1 |
| + |
PPP2CA | down-regulates activity
dephosphorylation
|
DCK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275803 |
Ser74 |
EFEELTMsQKNGGNV |
|
|
| pmid |
sentence |
| 24462681 |
Protein phosphatase 2A regulates deoxycytidine kinase activity via Ser-74 dephosphorylation|Deoxycytidine kinase (dCK) is a critical enzyme for activation of anticancer nucleoside analogs. Its activity is controlled via Ser-74 phosphorylation. Here, we investigated which Ser/Thr phosphatase dephosphorylates Ser-74. In cells, the PP1/PP2A inhibitor okadaic acid increased both dCK activity and Ser-74 phosphorylation |
|
| Publications: |
1 |
| + |
PP2Ca_R1A_Bd | down-regulates activity
dephosphorylation
|
DCK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275802 |
Ser74 |
EFEELTMsQKNGGNV |
|
|
| pmid |
sentence |
| 24462681 |
Protein phosphatase 2A regulates deoxycytidine kinase activity via Ser-74 dephosphorylation|Deoxycytidine kinase (dCK) is a critical enzyme for activation of anticancer nucleoside analogs. Its activity is controlled via Ser-74 phosphorylation. Here, we investigated which Ser/Thr phosphatase dephosphorylates Ser-74. In cells, the PP1/PP2A inhibitor okadaic acid increased both dCK activity and Ser-74 phosphorylation |
|
| Publications: |
1 |
| + |
DCK | up-regulates quantity
chemical modification
|
2'-deoxyguanosine 5'-monophosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275809 |
|
|
|
|
| pmid |
sentence |
| 20637175 |
Human deoxycytidine kinase (dCK4; EC 2.7.1.74) catalyzes the phosphorylation of 2′-deoxycytidine (dCyd), 2′-deoxyadenosine and 2′-deoxyguanosine to their corresponding monophosphate forms, using ATP or UTP as phosphoryl donors. This reaction is the first and rate-limiting step of the deoxyribonucleoside salvage pathway, which provides deoxynucleoside triphosphates for DNA replication and repair as an alternative to de novo nucleotide synthesis |
|
| Publications: |
1 |
| + |
DCK | up-regulates quantity
chemical modification
|
2'-deoxyadenosine 5'-monophosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275808 |
|
|
|
|
| pmid |
sentence |
| 20637175 |
Human deoxycytidine kinase (dCK4; EC 2.7.1.74) catalyzes the phosphorylation of 2′-deoxycytidine (dCyd), 2′-deoxyadenosine and 2′-deoxyguanosine to their corresponding monophosphate forms, using ATP or UTP as phosphoryl donors. This reaction is the first and rate-limiting step of the deoxyribonucleoside salvage pathway, which provides deoxynucleoside triphosphates for DNA replication and repair as an alternative to de novo nucleotide synthesis |
|
| Publications: |
1 |
| + |
DCK | up-regulates quantity
chemical modification
|
2'-deoxycytosine 5'-monophosphate(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275807 |
|
|
|
|
| pmid |
sentence |
| 20637175 |
Human deoxycytidine kinase (dCK4; EC 2.7.1.74) catalyzes the phosphorylation of 2′-deoxycytidine (dCyd), 2′-deoxyadenosine and 2′-deoxyguanosine to their corresponding monophosphate forms, using ATP or UTP as phosphoryl donors. This reaction is the first and rate-limiting step of the deoxyribonucleoside salvage pathway, which provides deoxynucleoside triphosphates for DNA replication and repair as an alternative to de novo nucleotide synthesis |
|
| Publications: |
1 |
| + |
DCK | down-regulates activity
binding
|
CDK1 |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275805 |
|
|
|
|
| pmid |
sentence |
| 22850745 |
We demonstrate that dCK interacts with cyclin-dependent kinase 1 (Cdk1) after IR and that the interaction inhibits Cdk1 activity both in vitro and in vivo. |
|
| Publications: |
1 |
3.0
DCK
- 
- 